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Related Experiment Videos

Proteolytic activity in the insulin receptor.

E C Vega-SaenzdeMiera1, B Rubalcava

  • 1Departamento de Bioquimica, Centro de Investigacion y de Estudios, Avanzados del Instituto Politecnico Nacional, Mexico, D.F.

Biochemical and Biophysical Research Communications
|October 14, 1988
PubMed
Summary

The insulin receptor, when activated by trypsin, exhibits protease activity specific to arginine. Insulin enhances this esterase activity, suggesting the receptor may be a zymogen involved in insulin signaling.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Background:

  • The insulin receptor plays a crucial role in mediating insulin's cellular effects.
  • Understanding the molecular mechanisms of insulin receptor activation and function is essential for deciphering metabolic regulation.

Purpose of the Study:

  • To investigate the enzymatic activity of the purified rat liver insulin receptor.
  • To determine if the insulin receptor possesses intrinsic proteolytic or esterase activity.
  • To explore the influence of insulin on the receptor's enzymatic properties.

Main Methods:

  • Purification of rat liver insulin receptor.
  • Incubation of the purified receptor with trypsin and synthetic protease substrates.
  • Assay of hydrolytic activity using specific substrates (e.g., N alpha-benzoyl-L-arginine ethyl ester).

Related Experiment Videos

  • Inhibition studies using soybean trypsin inhibitor and N alpha-p-tosyl-L-lysil chloromethyl ketone.
  • Investigation of insulin's effect on esterase activity.

    • Main Results:

    • The purified insulin receptor, upon activation by trypsin, demonstrated hydrolytic activity against arginine-containing substrates.
    • This activity was inhibited by soybean trypsin inhibitor, indicating a trypsin-like protease.
    • Insulin significantly enhanced the esterase activity of the trypsin-activated receptor.
    • The insulin concentration for half-maximal stimulation correlated with the receptor's dissociation constant.

    Conclusions:

    • The insulin receptor exhibits trypsin-activated proteolytic activity specific for arginine residues.
    • Insulin binding potentiates this enzymatic activity.
    • These findings suggest the insulin receptor may function as a zymogen, potentially releasing a peptide mediator of insulin's intracellular actions.